5vbg

Crystal Structure of full-length LpoA, Monoclinic form 1, from Haemophilus influenzae

spinqualitylabelsall models 5vbg, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vbg is a 1 chain structure with sequence from Haemophilus influenzae Rd KW20. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: CL, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LPOA_HAEIN Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a). Publication Abstract from PubMed In many Gram-negative bacteria, the peptidoglycan synthase PBP1A requires the outer membrane lipoprotein LpoA for constructing a functional peptidoglycan required for bacterial viability. Previously, we have shown that the C-terminal domain of Haemophilus influenzae LpoA (HiLpoA) has a highly conserved, putative substrate-binding cleft between two alpha/beta lobes. Here, we report a 2.0-A-resolution crystal structure of the HiLpoA N-terminal domain. Two subdomains contain tetratricopeptide-like motifs that form a concave groove, but their relative orientation differs by ~45 degrees from that observed in an NMR structure of the Escherichia coli LpoA N domain. We also determined three 2.0-2.8-A-resolution crystal structures containing four independent full-length HiLpoA molecules. In contrast to an elongated model previously suggested for E. coli LpoA, each HiLpoA formed a U-shaped structure with a different C-domain orientation. This resulted from both N-domain twisting and rotation of the C domain (up to 30 degrees ) at the end of the relatively immobile interdomain linker. Moreover, a previously predicted hinge between the lobes of the LpoA C domain exhibited variations of up to 12 degrees . Small-angle X-ray scattering (SAXS) data revealed excellent agreement with a model calculated by normal mode analysis (NMA) from one of the full-length HiLpoA molecules, but even better agreement with an ensemble of this molecule and two of the partially extended NMA-predicted models. The different LpoA structures helped explain how an outer membrane-anchored LpoA can either withdraw from or extend toward the inner membrane-bound PBP1A through peptidoglycan gaps and hence regulate the synthesis of peptidoglycan necessary for bacterial viability. Structural analyses of the Haemophilus influenzae peptidoglycan synthase activator LpoA suggest multiple conformations in solution.,Sathiyamoorthy K, Vijayalakshmi J, Tirupati B, Fan L, Saper MA J Biol Chem. 2017 Sep 8. pii: jbc.M117.804997. doi: 10.1074/jbc.M117.804997. PMID:28887305 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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